6e6t

Dieckmann cyclase, NcmC, bound to cerulenin

spinqualitylabelsall models 6e6t, resolution 1.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6e6t is a 2 chain structure with sequence from Saccharothrix syringae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.6Å Ligands: HVV, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A1X9WEN9_SACSY Publication Abstract from PubMed While several bioactive natural products that contain tetramate or pyridone heterocycles have been described, information on the enzymology underpinning these functionalities has been limited. Here we biochemically characterize an off-loading Dieckmann cyclase, NcmC, that installs the tetramate headgroup in nocamycin, a hybrid polyketide/nonribosomal peptide natural product. Crystal structures of the enzyme (1.6 A) and its covalent complex with the epoxide cerulenin (1.6 A) guide additional structure-based mutagenesis and product-profile analyses. Our results offer mechanistic insights into how the conserved thioesterase-like scaffold has been adapted to perform a new chemical reaction, namely, heterocyclization. Additional bioinformatics combined with docking and modeling identifies likely candidates for heterocycle formation in underexplored gene clusters and uncovers a modular basis of substrate recognition by the two subdomains of these Dieckmann cyclases. Structural Basis for Enzymatic Off-Loading of Hybrid Polyketides by Dieckmann Condensation.,Cogan DP, Ly J, Nair SK ACS Chem Biol. 2020 Oct 16;15(10):2783-2791. doi: 10.1021/acschembio.0c00579., Epub 2020 Oct 5. PMID:33017142 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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